Characterization of GmCaMK1, a member of a soybean calmodulin-binding receptor-like kinase family
Date
2010
Authors
DeFalco, T.
Chiasson, D.
Munro, K.
Kaiser, B.
Snedden, W.
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Journal article
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FEBS Letters, 2010; 584(23):4717-4724
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Thomas A. DeFalco, David Chiasson, Kim Munro, Brent N. Kaiser and Wayne A. Snedden
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Abstract
Calmodulin(CaM)-regulated protein phosphorylation forms an important component of Ca(2+) signaling in animals but is less understood in plants. We have identified a CaM-binding receptor-like kinase from soybean nodules, GmCaMK1, a homolog of Arabidopsis CRLK1. We delineated the CaM-binding domain (CaMBD) of GmCaMK1 to a 24-residue region near the C-terminus, which overlaps with the kinase domain. We have demonstrated that GmCaMK1 binds CaM with high affinity in a Ca(2+)-dependent manner. We showed that GmCaMK1 is expressed broadly across tissues and is enriched in roots and developing nodules. Finally, we examined the CaMBDs of the five-member GmCaMK family in soybean, and orthologs present across taxa.
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Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.